Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 Å resolution. Conservation of solvent sites in RNase-A high-resolution structures
- 1 November 1993
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 49 (6) , 541-547
- https://doi.org/10.1107/s090744499300719x
Abstract
The X-ray structure of the inhibitor complex of bovine ribonuclease A with cytidylic acid (2'-CMP) has been determined at 1.6 A resolution and refined by restrained least squares to R = 0.17 for 11 945 reflections. Binding of the inhibitor molecule to the protein is confirmed to be in the productive mode associated with enzyme activity. A study of conserved solvent sites amongst high-resolution structures in the same crystal form reveals a stabilizing water cluster between the N and C termini.Keywords
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